The objective of this work is to describe in detail the structure-function biochemistry of bacterial neuraminidases. Homogeneous neuraminidase will be isolated from the soil microorganism Arthrobacter, which was obtained by elective culture. Our immediate goal is to determine such physical and chemical properties of the enzyme as the C-and N- terminal amino acids, subunit structure, and carbohydrate content and location on the protein chain. The mechanism of action of Arthrobacter neuraminidase will be investigated by determining the amino acid residues at the active site by the use of conventional group-specific and site-directing irreversible inhibitors. The latter compounds may have potential chemotherapeutic value in the treatment of such infectious diseases as influenza and bacterial pneumonia. A corollary objective is the preparation of immobilized neuraminidase and comparison of its physical and chemical properties to those of the unbound form. In addition, the potential use of the immobilized enzyme will be investigated as a means to selectively remove sialic acid residues from the cell membrane of normal and malignant cells. BIBLIOGRAPHIC REFERENCES: "Properties of Arthrobacter Neuraminidase" (Abstract), M. Flashner, P. Wang and S.W. Tanenbaum, submitted to FASEB (San Francisco, Calif., June 6-10, 1976).